An aminopeptidase from bovine brain which catalyzes the hydrolysis of the tyrosyl1‐glycine2 bond of methionine5‐enkephalin has been purified to electrophoretic homogeneity. The enzyme also catalyzes the hydrolysis of di‐peptides, tripeptides, and amino acid β‐naphthylamides. The enzyme can be inactivated by dialysis against EDTA, and reconstituted with divalent metal ions. Inhibition of the enzyme is observed in the presence of p‐chloromercuribenzoate and puromycin, the latter compound not being hydro‐lyzed by the enzyme. The enzyme is composed of a single polypeptide chain of molecular weight approx. 100,000. The properties of this enzyme are similar to those reported for other brain aminopeptidases active on enkephalin, although distinct differences are observed.
|Number of pages||8|
|Journal||Journal of Neurochemistry|
|State||Published - Jan 1981|
- Enkephalin hydrolysis
- Substrate specificity
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience